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Literature summary for 3.6.4.B10 extracted from

  • Zako, T.; Sahlan, M.; Fujii, S.; Yamamoto, Y.Y.; Tai, P.T.; Sakai, K.; Maeda, M.; Yohda, M.
    Contribution of the C-terminal region of a group II chaperonin to its interaction with prefoldin and substrate transfer (2016), J. Mol. Biol., 428, 2405-2417 .
    View publication on PubMed
Search for more literature for 3.6.4.B10

Protein Variants

Protein Variants Comment Organism
additional information construction of three CPNbeta mutants, with the truncation of 1, 2 and 6 amino acids from the C-terminus, named CPNbetaTc1, CPNbetaTc2 and CPNbetaTc6, respectively. CPNbetaTc2 and CPNbetaTc6 are designed to delete two hydrophobic amino acid residues from the CPNbeta C-terminus (Gly-Ser-Glu-Asp-/Phe-Gly-Ser-Asp-/Leu-Asp, with / indicating Tc6 and Tc2 truncation positions). The mutants form hexadecameric homooligomers, similar to the wild-type CPNbeta (CPNbetaWT). The thermal aggregation of CS is completely suppressed by the presence of an equimolar amount of the CPNbeta mutant variants. The truncation mutants exhibit the same protection abilities as CPNbetaWT. The mutant isoforms CPNbeta and PFDalpha1beta1 from strain KS1 interact with each other at high affinity, interaction analysis using immobilized PFDalpha1beta1, overview Thermococcus sp. JCM 11816

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Thermococcus sp. JCM 11816 5829
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Thermococcus sp. JCM 11816

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Thermococcus sp. JCM 11816
-
 ADP + phosphate
-
 ?
additional information Thermococcus sp. JCM 11816 the enzyme assists in folding of IPMDH ?
-
-

Organism

Organism UniProt Comment Textmining
Thermococcus sp. JCM 11816 P61112 AND O24730 thermosome subunits alpha and beta; KS-1
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
 Thermococcus sp. JCM 11816 ADP + phosphate
-
 ?
additional information the enzyme assists in folding of IPMDH Thermococcus sp. JCM 11816 ?
-
-

Subunits

Subunits Comment Organism
hexadecamer
-
 Thermococcus sp. JCM 11816

Synonyms

Synonyms Comment Organism
group II chaperonin
-
 Thermococcus sp. JCM 11816
group II CPN
-
 Thermococcus sp. JCM 11816
thermosome
-
 Thermococcus sp. JCM 11816

Cofactor

Cofactor Comment Organism Structure
additional information the group II CPNs do not require a GroES-like co-CPN but have a built-in lid that is composed of a helical protrusion in the apical domain. The rate of transfer of a substrate protein from PFD to CPN correlates with the strength of the PFD-CPN interaction Thermococcus sp. JCM 11816
prefoldin PFD, is a jellyfish-like hexameric protein that is exclusively found in archaea and eukaryotes, ans is a molecular chaperone that captures an unfolded protein substrate and transfers it to a group II chaperonin (CPN). The transfer of a substrate from PFD to CPN involves a direct interaction, PFD interacts with the apical domain of CPN. Analysis of protein-folding mechanism of PFD and CPN using the PFD-CPN systems of the hyperthermophilic archaea, the C-terminal region contributes to the functional cooperation between PFDalpha1beta1 and CPNbeta, overview. The C-terminus of the PFD alpha subunit is not important for the interaction with CPN and substrate transfer Thermococcus sp. JCM 11816

General Information

General Information Comment Organism
evolution chaperonins (CPNs) are subdivided into group I and group II. Group I CPNs are present in bacteria and in the organelles of eukaryotes. Group II CPNs exist in the cytosol of archaea and eukaryotes Thermococcus sp. JCM 11816
additional information analysis of molecular mechanisms of group II CPNs, ATP is involved in the protein folding inducing conformational changes of substrate and enzyme, overview Thermococcus sp. JCM 11816
physiological function chaperonins (CPNs) are ubiquitous, double ring-shaped molecular chaperones that capture unfolded proteins in their cavities and assist in protein folding in an ATP-dependent manner. Prefoldin (PFD) captures an unfolded protein substrate and transfers it to a group II chaperonin (CPN). The transfer of a substrate from PFD to CPN involves a direct interaction, PFD interacts with the apical domain of CPN, analysis of protein-folding mechanism of PFD and CPN using the PFD-CPN systems of the hyperthermophilic archaea, overview Thermococcus sp. JCM 11816